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  • 1
    Electronic Resource
    Electronic Resource
    Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy (1991)
    Springer
    Journal of biomolecular NMR 1 (1991), S. 167-173 
    Details
    ISSN: 1573-5001
    Keywords: Channel structure ; Magainin ; Acetylcholine receptor ; Lipid bilayer ; Amphiphilic α-helix ; 15N chemical shift ; Solid-state NMR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Solid-state NMR spectroscopy was used to determine the orientations of two amphipathic helical peptides associated with lipid bilayers. A single spectral parameter provides sufficient orientational information for these peptides, which are known, from other methods, to be helical. The orientations of the peptides were determined using the15N chemical shift observed for specifically labeled peptide sites. Magainin, an antibiotic peptide from frog skin, was found to lie in the plane of the bilayer. M2δ, a helical segment of the nicotinic acetylcholine receptor, was found to span the membrane, perpendicular to the plane of the bilayer. These findings have important implications for the mechanisms of biological functions of these peptides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01877228
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  • 2
    Electronic Resource
    Electronic Resource
    Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers (1995)
    Springer
    Journal of biomolecular NMR 6 (1995), S. 329-334 
    Details
    ISSN: 1573-5001
    Keywords: Solid-state NMR ; Magainin ; Membranes ; Oriented samples ; Structure determination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A three-dimensional 1H chemical shift/1H-15N dipolar coupling/15N chemical shift correlation spectrum was obtained on a sample of specifically 15N-labeled magainin peptides oriented in lipid bilayers between glass plates in a flat-coil probe. The spectrum showed complete resolution of the resonances from two labeled amide sites in all three dimensions. The three orientationally dependent frequencies associated with each resonance enabled the orientation of the peptide planes to be determined relative to the direction of the applied magnetic field. These results demonstrate the feasibility of multiple-pulse spectroscopy in a flat-coil probe, the ability to measure three spectral parameters from each site in a single experiment, and the potential for resolving among many labeled sites in oriented membrane proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00197814
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    NMR of fd coat protein (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 11 (1979), S. 139-145 
    Details
    ISSN: 0091-7419
    Keywords: fd coat protein ; 1H NMR ; 13C NMR ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The conformations of the major coat protein of a filamentous bacteriophage can be described by nuclear magnetic resonance spectroscopy of the protein and the virus. The NMR experiments involve detection of the 13C and 1H nuclei of the coat protein. Both the 13C and 1H nuclear magnetic resonance (NMR) spectra show that regions of the polypeptide chain have substantially more motion than a typical globular protein. The fd coat protein was purified by gel chromatography of the SDS solubilized virus. Natural abundance 13C NMR spectra at 38 MHz resolve all of the nonprotonated aromatic carbons from the three phenylalanines, two tyrosines, and one tryptophan of the coat protein. The α carbons of the coat protein show at least two different classes of relaxation behavior, indicative of substantial variation in the motion of the backbone carbons in contrast to the rigidity of the α carbons of globular proteins. The 1H spectrum at 360 MHz shows all of the aromatic carbons and many of the amide protons. Titration of a 1H spectra gives the pKas for the tyrosines.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400110204
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    Paper (German National Licenses)
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